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SIRT5 is a human member of a family of proteins called Sirtuins (Sir2-like proteins) and are present in prokaryotes and eukaryotes. All Sir2-like proteins have a sirtuin core domain, which contains a series of sequence motifs conserved in organisms ranging from bacteria to humans. Bacterial, yeast and mammalian sirtuins are able to metabolize NAD and possibly at as mono-ADP-ribosyltransferases. The enzymatic function of sirtuins is not yet completely understood but recent reports of histone-activated Sir2-mediated NAD metabolism and NAD-activated Sir2-mediated histone deacetylation suggest a possible coupled reciprocal activation mechanism involving interactions of Sir2 with NAD and the N epsilon-acetyl-lysine groups of acetylated histones.
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Protein Aliases: NAD-dependent deacetylase sirtuin-5; NAD-dependent lysine demalonylase and desuccinylase sirtuin-5, mitochondrial; NAD-dependent protein deacylase sirtuin-5, mitochondrial; NAD-dependent protein deacylase sirtuin-5, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03160}; Regulatory protein SIR2 homolog 5; regulatory protein SIR2 homolog 5 {ECO:0000255|HAMAP-Rule:MF_03160}; silent mating type information regulation 2, S.cerevisiae, homolog 5; SIR2 like protein 5; sir2-like 5; SIR2-like protein 5; SIR2-like protein 5 {ECO:0000255|HAMAP-Rule:MF_03160}; SIR2L5; SIRT5; sirtuin type 5
Gene Aliases: 0610012J09Rik; 1500032M05Rik; AV001953; SIR2L5; SIRT5
UniProt ID: (Human) Q9NXA8, (Mouse) Q8K2C6, (Rat) Q68FX9
Entrez Gene ID: (Human) 23408, (Mouse) 68346, (Rat) 306840
Molecular Function:
DNA binding protein
chromatin/chromatin-binding protein
deacetylase
hydrolase
nucleic acid binding
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